HIST1H2AE

H2AC8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CV5, 3A6N, 3AFA, 3AN2, 3AV1, 3AV2, 3AYW, 3AZE, 3AZF, 3AZG, 3AZH, 3AZI, 3AZJ, 3AZK, 3AZL, 3AZM, 3AZN, 3W96, 3W97, 3W98, 3W99, 3WKJ, 3WTP, 5CPJ, 5B0Z, 4YM5, 5AV9, 5AVB, 5AV5, 4YM6, 5CPI, 3X1V, 5AV6, 3X1S, 5AV8, 5CPK, 5AVC, 5B0Y, 4Z5T, 5B24, 2RVQ, 5B40, 5AY8, 5B2I, 5B2J
Identifiers
Aliases	H2AC8, H2A.1, H2A.2, H2A/a, H2AFA, histone cluster 1, H2ae, histone cluster 1 H2A family member e, HIST1H2AE, H2A clustered histone 8, H2AC4
External IDs	OMIM: 602786 MGI: 2448457 HomoloGene: 135791 GeneCards: H2AC8
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.2 Start 26,216,975 bp End 26,217,483 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 21,900,592 bp End 21,900,984 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon monocyte bone marrow cells right uterine tube prostate amniotic fluid corpus epididymis blood skin of abdomen vagina Top expressed in uterus spermatid yolk sac bone marrow mesencephalon neural tube thymus spermatocyte morula stomach More reference expression data BioGPS n/a
Gene ontology Molecular function DNA binding protein heterodimerization activity protein binding Cellular component nucleosome extracellular exosome nucleus chromosome Biological process negative regulation of cell population proliferation chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3012 319191 Ensembl ENSG00000277075 ENSMUSG00000071516 UniProt P04908 C0HKE2 B2RVF0 C0HKE1 C0HKE3 C0HKE5 C0HKE4 C0HKE6 C0HKE7 C0HKE8 C0HKE9 RefSeq (mRNA) NM_021052 NM_178182 RefSeq (protein) NP_003504 NP_835496 NP_835495 NP_835494 NP_835491 NP_835489 NP_783591 NP_835493 NP_835496 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835489 NP_001171015 NP_835496 NP_835491 NP_835493 NP_835494 NP_835495 NP_835492 NP_783591 NP_835495 NP_835489 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835494 NP_835489 NP_835495 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835492 NP_835491 NP_835489 NP_835495 NP_835494 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835491 NP_835489 NP_835495 NP_835494 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 Location (UCSC) Chr 6: 26.22 – 26.22 Mb Chr 13: 21.9 – 21.9 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene.

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4).

The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.

Further reading

• Rodriguez P, Munroe D, Prawitt D, et al. (1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". Genomics. 44 (3): 253–65. doi:10.1006/geno.1997.4868. PMID 9325046.
• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656. S2CID 38539096.
• El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter". Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
• Deng L, de la Fuente C, Fu P, et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones". Virology. 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
• Deng L, Wang D, de la Fuente C, et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology. 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
• Galasinski SC, Louie DF, Gloor KK, et al. (2002). "Global regulation of post-translational modifications on core histones". J. Biol. Chem. 277 (4): 2579–88. doi:10.1074/jbc.M107894200. PMID 11709551.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
• Zhang Y, Griffin K, Mondal N, Parvin JD (2004). "Phosphorylation of histone H2A inhibits transcription on chromatin templates". J. Biol. Chem. 279 (21): 21866–72. doi:10.1074/jbc.M400099200. PMID 15010469.
• Aihara H, Nakagawa T, Yasui K, et al. (2004). "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo". Genes Dev. 18 (8): 877–88. doi:10.1101/gad.1184604. PMC 395847. PMID 15078818.
• Wang H, Wang L, Erdjument-Bromage H, et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature. 431 (7010): 873–8. Bibcode:2004Natur.431..873W. doi:10.1038/nature02985. PMID 15386022. S2CID 4344378.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Hagiwara T, Hidaka Y, Yamada M (2005). "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes". Biochemistry. 44 (15): 5827–34. doi:10.1021/bi047505c. PMID 15823041.
• Bonenfant D, Coulot M, Towbin H, et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry". Mol. Cell. Proteomics. 5 (3): 541–52. doi:10.1074/mcp.M500288-MCP200. PMID 16319397.
• Cao R, Tsukada Y, Zhang Y (2006). "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing". Mol. Cell. 20 (6): 845–54. doi:10.1016/j.molcel.2005.12.002. PMID 16359901.
• Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL (2006). "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. doi:10.1021/pr050269n. PMID 16457589.